title: Methylthioadenosine nucleosidase in normal and dystrophic human muscle.
abstract: Human skeletal muscle homogenate was found to contain a nucleosidase that catalyzes the hydrolysis of 5'-methylthioadenosine, a known inhibitor of many methyl transfer reactions. When the levels of methylthioadenosine nucleosidase in muscle of patients were compared with those of controls, no significant alterations in its activity were noted in patients with various forms of muscular dystrophies, polymyositis and certain denervating diseases.
mesh_terms: D000241:Adenosine / Q000031:analogs & derivatives / Q000378:metabolism; D006801:Humans; D009132:Muscles / Q000201:enzymology*; D009136:Muscular Dystrophies / Q000201:enzymology*; D009220:Myositis / Q000201:enzymology; D009468:Neuromuscular Diseases / Q000201:enzymology; D010430:Pentosyltransferases / Q000378:metabolism*; D011683:Purine-Nucleoside Phosphorylase / Q000378:metabolism*; D013872:Thionucleosides / Q000378:metabolism
chemical_list: D013872:Thionucleosides; D010430:Pentosyltransferases; D011683:Purine-Nucleoside Phosphorylase; C021784:5'-methylthioadenosine phosphorylase; D000241:Adenosine